Synthesis, structures and Helicobacter pylori urease inhibitory activity of copper(II) complexes with tridentate aroylhydrazone ligands.

Synthesis, structures and urease inhibitory activity of cobalt(III) complexes with Schiff bases.

Nine new copper(II) complexes derived from various Schiff bases were prepared. They are [Cu2Br2(L1)2] (1), [Cu(L2)2]·2NO3·2CH3OH (2), [Cu(L3)2]·2Br (3), [Cu(L4)2] (4), [Cu2Cl4(L2)2] (5), [Cu2Cl2(L5)2] (6), [CuL6(NCS)] (7), [CuClL6]·CH3OH (8), and [Cu2(L7)2] (9), where L1 is the monoanionic form of 2-chloro-N′-(4-diethylamino-2-hydroxybenzylidene)benzohydrazide (HL1), L2 is the zwitterionic form of 4-methyl-2-((3-morpholinopropylimino)methyl)phenol (L2), L3 is the zwitterionic form of 2-bromo-4-chloro-6-((2-(2-hydroxyethylamino)ethylimino)methyl)phenol (L3), L4 is the monoanionic form of 2-bromo-4-chloro-6-((cyclopentylimino)methyl)phenol (HL4), L5 is the monoanionic form of 2-((cyclopropylimino)methyl)-4-methylphenol (HL5), L6 is the monoanionic form of 4-methyl-2-((pyridin-2-ylmethylimino)methyl)phenol (HL6), and L7 is the dianionic form of N,N′-bis(5-methylsalicylidene)-1,4-diiminobutane (H2L7). The complexes were characterized by infrared and UV-Vis spectra, and single crystal X-ray diffraction. The Cu atoms in complex 1 display square pyramidal coordination, in complex 5 display trigonal bipyramidal coordination, in complex 9 show tetrahedrally distorted square planar coordination, and in the remaining complexes display square planar coordination. Complexes 2, 3, 5, 7 and 8 show effective urease inhibitory activities, with IC50 values of 0.37 ± 1.22, 0.21 ± 0.97, 0.03 ± 0.78, 0.39 ± 0.58 and 0.76 ± 0.95 μM, respectively. Molecular docking study of the complexes with Helicobacter pylori urease was performed. Complex 5 has the most effective activity against urease, with a mixed competitive inhibition mechanism. The complex interacts with the nickel atom of the urease active center, and with the remaining parts of the complex molecule block the entrance of the urease active pocket.

Inhibition studies of Helicobacter pylori urease with Schiff base copper(II) complexes

Background and the purpose of the study: Helicobacter pylori (H. pylori) infection leads to different clinical and pathological outcomes in humans, including chronic gastritis, peptic ulcer disease and gastric neoplasia and even gastric cancer and its eradiation depends upon multi-drug therapy. The most effective therapy is still unknown and prompts people to make great efforts to find better and more modern natural or synthetic anti-H. pylori agents.
Methods: In this report 21 randomly selected herbal methanolic extracts were evaluated for their effect on inhibition of Jack-bean urease using the indophenol method as described by Weatherburn. The inhibition potency was measured by UV spectroscopy technique at 630 nm which attributes to released ammonium.
Results: Among these extracts, five showed potent inhibitory activities with IC50 ranges of 18-35 µg/mL. These plants are Matricaria disciforme (IC50=35 µg/mL), Nasturtium officinal (IC50=18 µg/mL), Punica granatum (IC50=30 µg/mL), Camelia sinensis (IC50=35 µg/mL), Citrus aurantifolia (IC50=28 µg/mL).
Conclusion: Medicinal plants, traditional medicinal and other natural sources are still good source for lead discovery. The results of this study revealed that random screening of medicinal plants could lead to introducing new candidate for further studies which, in the end, can help and enhance human health.

A Preliminary Investigation of the Jack-Bean Urease Inhibition by Randomly Selected Traditionally Used Herbal Medicine

Urease plays a significant role in the pathogenesis of several diseases and also has practical implications in other fields, such as agriculture or chemical analysis. Among the multitude of chemical species known to inhibit urease, metal complexes stand out as a special category due to their specific mechanism of action, distinct from purely organic substances. Their inhibitory activity seems to depend on the type of metal and its oxidation state as well as on the coordination environment of the central atom. Furthermore, the study of the interaction between metal ions and their complexes with urease renders valuable insights into detailed catalytic mechanisms of this enzyme. This brief survey attempts to provide an overview of the published research on urease inhibition by metal complexes.

REVIEW: metal complexes as urease inhibitors

Synthesis, structures and urease inhibition studies of dimeric copper(II) complexes of Schiff bases derived from glycine

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Synthesis, structures and urease inhibition studies of dimeric copper(II) complexes of Schiff bases derived from glycine